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Crystal structure of putative Chitinase A from Streptomyces coelicolor.

Analyse Crystal structure of putative Chitinase A from Streptomyces coelicolor. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3EBV
Type
protein
Length
293 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.5
Source
Streptomyces coelicolor
Molecule
Chinitase A
UniProt
Q9KY99
Ligands
SO4
Pockets
1 · best druggability 0.47

Structure

x-ray diffraction · resolution 1.5 · 1 distinct chain · 37% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AChinitase Aprotein29337% helix, 19% strandQ9KY99

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11250.470.7828empty

Modifications

Observed in the structure: 8 modified, 2 disulfide (engineered, disulfide).

Compared structures

  • 3EBV · Crystal structure of putative chitinase a from streptomyces coelicolor. · the same entry in another collection · chain A against A, TM-score 1.00

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